Computer simulations of prebiotic evolution
- Harvard Univ., Cambridge, MA (United States)
This paper is a review of our previous work on the field of possible ways of prebiotic evolution. We propose an algorithm providing sequences of model proteins with rapid folding into a given native conformation. Thermodynamical analysis shows that the increase in speed is matched by an increase in stability: the evolved sequences are much more stable in their native conformation than the initial random sequence. We discuss a possible origin of the first biopolymers, having stable unique structure. We suggest that at the prebiotic stage of evolution, long organic polymers had to be compact in order to avoid hydrolysis and had to be soluble and thus must not be exceedingly hydrophobic. We present an algorithm that generates such sequences of model proteins. The evolved sequences turn out to have a stable unique structure, into which they quickly fold. This result illustrates the idea that the unique three-dimensional native structure of first biopolymers could have evolved as a side effect of a nonspecific physico-chemical factors acting at the prebiotic stage of evolution. 21 refs., 5 figs.
- OSTI ID:
- 549238
- Report Number(s):
- CONF-970132-; TRN: 97:005592-0008
- Resource Relation:
- Conference: Pacific symposium on biocomputing `97, Kapalua, HI (United States), 6-9 Jan 1997; Other Information: PBD: 1996; Related Information: Is Part Of Pacific symposium on biocomputing `97: Proceedings; Altman, R.B. [ed.] [Stanford Univ., CA (United States). Section on Medical Informatics]; Dunker, A.K. [ed.] [Washington State Univ., Pullman, WA (United States). Dept. of Biochemistry and Biophysics]; Hunter, L. [ed.] [National Insts. of Health, Bethesda, MD (United States). National Library of Medicine]; Klein, T.E. [ed.] [California Univ., San Francisco, CA (United States). Dept. of Pharmaceutical Chemistry]; PB: 508 p.
- Country of Publication:
- United States
- Language:
- English
Similar Records
Protein structure prediction and potential energy landscape analysis using continuous global minimization
PROTEIN QUALITY CONTROL IN BACTERIAL CELLS: INTEGRATED NETWORKS OF CHAPERONES AND ATP-DEPENDENT PROTEASES.
Related Subjects
BASIC STUDIES
99 MATHEMATICS
COMPUTERS
INFORMATION SCIENCE
MANAGEMENT
LAW
MISCELLANEOUS
ORGANIC POLYMERS
BIOLOGICAL EVOLUTION
PROTEINS
HYDROLYSIS
DNA SEQUENCING
STABILITY
THERMODYNAMIC PROPERTIES
CONFORMATIONAL CHANGES
STRUCTURE-ACTIVITY RELATIONSHIPS
MUTATIONS
ELECTRONIC STRUCTURE
COMPUTERIZED SIMULATION
ALGORITHMS
MONTE CARLO METHOD
STATISTICAL MODELS
FREE ENERGY